Disease relevance of copper cation

• This result indicated that the apparent cuprous ion toxicity was not due to excess intracellular copper [1].
• Copper(I), copper(II) and silver ions have been shown to be potent inhibitors of purified soluble methane monooxygenase (MMO) of Methylococcus capsulatus (Bath) [2].
• Distribution of metallothionein (MT) and copper ion (Cu) in the liver of LEC (Long-Evans Cinnamon) rats was investigated to examine the relationship between Cu-MT induction and the development of hepatitis followed by hepatocellular carcinomas [3].
• Stannous and cuprous ion oxidation by Thiobacillus ferrooxidans [4].

High impact information on copper cation

• It possesses a long N-terminal tail protruding into the cytosol and containing six copper(I)-binding domains, which are individually folded and capable of binding one copper(I) ion [5].
• Yeast cox17 solution structure and Copper(I) binding [6].
• In contrast, the specific cuprous ion chelator neocuproine (2,9-dimethyl-1,10-phenanthroline), as well as other copper-chelating agents, did not protect against H(2)O(2)-induced cellular DNA damage [7].
• Finally, oxidation of Cu(2+) to Cu(3+) has been studied by cyclic voltammetry in water, which revealed that the redox reaction occurs only when the copper cation is within the diamino-diimido compartment [8].
• These results demonstrate that DMT1 is a physiologically relevant Cu(1+) transporter in intestinal cells, indicating that intestinal absorption of copper and iron are intertwined [9].

Biological context of copper cation

• The enzymes may play an essential role in copper homeostasis since they exhibit a strikingly similar kinetic activity towards Cu(1+) as substrate [10].
• Copper(I) complexes of a heavily fluorinated beta-diketiminate ligand: synthesis, electronic properties, and intramolecular aerobic hydroxylation [11].
• It was concluded that alpha-tocopherol reacts with free copper(II) ion to give more reactive copper(I) ion and may act as a prooxidant for lipid peroxidation in the presence of free copper ion [12].
• The molecular structures show that copper(II) ions in an asymmetrically elongated octahedral coordination (type 4 + 1 + 1) and in binuclear complex Cu(1) atom has a asymmetrically elongated octahedral coordination (type type 4 + 1 + 1) and Cu(2) atom exhibits a square base pyramidal coordination (type 4 + 1) [13].

Associations of copper cation with other chemical compounds

• Analyses of the neutron powder diffraction reveal an ordered magnetic state where the moment of Cu(1) is antiparallel to those of the two Cu(2); all of them point along the a axis without any sign of geometrical frustration [14].
• Hydroxyl radical formation from cuprous ion and hydrogen peroxide: a spin-trapping study [15].
• Ag(1)(), Cu(1)(), and Cu(2)() exhibit blue pyrazole-based structured emissions with short phosphorescence lifetimes, 10(1)-10(2) micros, due to an internal heavy-metal effect [16].
• The X-ray structure determination of a complex formed between the C(2)-symmetric 2,2'-bipyridyl ligand (R = Ph) and copper(i) chloride showed that two bipyridyl ligands had coordinated to the copper(i) ion [17].

Gene context of copper cation

• PDTC concomitantly increased the intracellular levels of copper, and bathocuproinedisulfonic acid, a non-cell-permeable chelator of Cu(1+), inhibited the PDTC-induced increase in intracellular copper level and reversed the PDTC effects on IkappaB-alpha, NF-kappaB, and MCP-1 [18].
• Antioxidant capacity micromol/L) was evaluated by measuring the cuprous ion deriving from a known amount of cupric ion [19].
• Copper(I) interaction with model peptides of WD6 and TM6 domains of Wilson ATPase: regulatory and mechanistic implications [20].

References